1. Volume 2, Issue 1, Pages 141-147 (July 1998)
Function of Hexameric RNA in Packaging of Bacteriophage φ29 DNA In Vitro 
Feng Zhang, Sébastien Lemieux, Xiling Wu, Daniel St.-Arnaud, Cynthia T. McMurray, François Major, Dwight Anderson 
Molecular Cell 
Volume 2, Issue 1, Pages (July 1998)
DOI: /S (00)

2. Figure 1 Secondary Structure and Sequence Alignment of pRNAs
(a) Secondary structure of the 120-base form of wild-type pRNA (Bailey et al. 1990; Reid et al. 1994c). The line shows the proposed tertiary interaction. Helices are designated A, C, D, E, and G. The prohead binding domain (Reid et al. 1994a) is marked by shading.
(b) Phylogenetic sequence alignment of φ29 and related phage pRNAs that includes the sequence of domain I for each RNA (Bailey et al. 1990; Reid et al. 1994c). Helical regions are boxed and designated by capital letters. The tertiary interaction is shaded and designated by G and G′.
Molecular Cell 1998 2, DOI: ( /S (00) )

3. Figure 2
Mutagenesis, Gel Electrophoresis, and DNA Packaging to Test and Characterize the G Helix Interaction
(a) Sequence changes of mutants F6, F7, and F6/F7 are boxed, and the line shows the tertiary interaction.
(b) In vitro DNA–gp3 packaging activity of RNA-free proheads reconstituted with wild-type or mutant pRNAs. Lane 1 shows the DNA–gp3 added to each reaction (Input DNA). Lanes 2–7 show DNA–gp3 packaged by proheads reconstituted with the designated pRNA(s). Unpackaged DNA was digested with DNase; then, the packaged, DNase-resistant DNA–gp3 was extracted from filled heads and quantified following agarose gel electrophoresis.
(c) Native polyacrylamide gel electrophoresis of wild-type (wt) or mutant pRNA(s) at room temperature. The lanes contained 0.9 μg total of the designated pRNA(s).
(d) In vitro DNA–gp3 packaging activity of proheads reconstituted with wild-type or mutant pRNAs. Lane 1 shows the DNA–gp3 added to each reaction. Lanes 2–15 show DNA–gp3 packaged by proheads reconstituted with the designated pRNA(s). F6,F7 and F7,F6 refer to F6 followed by F7 or vice versa.
Molecular Cell 1998 2, DOI: ( /S (00) )

4. Figure 3
Molecular Mass of the Wild-Type and Mutant pRNAs in Solution Determined by Analytical Ultracentrifugation
(a) A representative concentration gradient formed from the wild-type (steep slope at the bottom of the cell) and the F6 and F7 mutants (superimposed curves) at 8,000 rpm, 4°C, and a sample concentration of 0.4 μM. A260 is the absorbance at 260 nm; R (cm) is the distance in centimeters from the solution/air meniscus toward the bottom of the cell.
(b) Results of the best fit to the data. The 4k, 8k, and 12k rpm speeds represent optimal equilibrium conditions for the hexamer, dimer and monomer, respectively; superscript (a), each concentration gradient was fit to both a single and a double component model. The best fit to the data is listed. In all cases, the data fit well to a single component or a double component but not both; superscript (b) (---) indicates that the data could not be fit. The F6 + F7 mixture contained equal concentrations (0.2 μM) of each RNA to obtain a final concentration of 0.4 μM.
(c) Native polyacrylamide gel electrophoresis of wild-type (wt) or mutant pRNA(s) at 4°C. The lanes contained 0.45 μg total of the designated pRNA(s). The fast, intermediate, and slow forms are hypothesized to be monomers (M), dimers (D), and hexamers (H), respectively.
Molecular Cell 1998 2, DOI: ( /S (00) )

5. Figure 4
Secondary Structure and Three-Dimensional Model of the pRNA Hexamer
(a) Secondary structure of the pRNA hexamer. The nucleotides of a construction subunit are shown in the shaded area. The transformation matrices, computed between the G37 bases, are indicated by the arrows. Watson-Crick base pairs are indicated by lines, and the wobble base pairs by dots. The residues required for intermolecular base pairing are boxed. Only residues 16–101, 5′ to 3′, of each 120-base molecule are shown. (M) designates the transformation matrix that links two consecutive monomers.
(b) Stereo view of the three-dimensional structure of the pRNA monomer. The intermolecular G stems are represented in red. The upper G stem connects monomers i and i+1. The lower right G stem connects monomers i-1 and i. All other stems are drawn in cyan. The incomplete lower right D stem is part of the monomer i-1. Single-stranded and unconstrained regions are shown in green. The Watson-Crick and wobble stem base pairs are indicated by small cylinders.
(c) Stereo view of the pRNA hexamer. A different color is assigned to each monomer. The four intermolecular Watson-Crick base pairs are represented by small cylinders. The images were generated by the program Ribbons, version 2.45, by Mike Carson at the University of Alabama at Birmingham, Center for Molecular Crystallography.
Molecular Cell 1998 2, DOI: ( /S (00) )

6. Figure 4
Secondary Structure and Three-Dimensional Model of the pRNA Hexamer
(a) Secondary structure of the pRNA hexamer. The nucleotides of a construction subunit are shown in the shaded area. The transformation matrices, computed between the G37 bases, are indicated by the arrows. Watson-Crick base pairs are indicated by lines, and the wobble base pairs by dots. The residues required for intermolecular base pairing are boxed. Only residues 16–101, 5′ to 3′, of each 120-base molecule are shown. (M) designates the transformation matrix that links two consecutive monomers.
(b) Stereo view of the three-dimensional structure of the pRNA monomer. The intermolecular G stems are represented in red. The upper G stem connects monomers i and i+1. The lower right G stem connects monomers i-1 and i. All other stems are drawn in cyan. The incomplete lower right D stem is part of the monomer i-1. Single-stranded and unconstrained regions are shown in green. The Watson-Crick and wobble stem base pairs are indicated by small cylinders.
(c) Stereo view of the pRNA hexamer. A different color is assigned to each monomer. The four intermolecular Watson-Crick base pairs are represented by small cylinders. The images were generated by the program Ribbons, version 2.45, by Mike Carson at the University of Alabama at Birmingham, Center for Molecular Crystallography.
Molecular Cell 1998 2, DOI: ( /S (00) )